ID H1Q4E8_9BACT Unreviewed; 407 AA.
AC H1Q4E8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHO67124.1};
GN ORFNames=HMPREF9140_01786 {ECO:0000313|EMBL:EHO67124.1};
OS Prevotella micans F0438.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=883158 {ECO:0000313|EMBL:EHO67124.1, ECO:0000313|Proteomes:UP000016023};
RN [1] {ECO:0000313|EMBL:EHO67124.1, ECO:0000313|Proteomes:UP000016023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0438 {ECO:0000313|EMBL:EHO67124.1,
RC ECO:0000313|Proteomes:UP000016023};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA Blanton J.M., Wade W.G., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella micans F0438.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the nicotinamide ribonucleoside (NR) uptake
CC permease (TC 4.B.1) family. {ECO:0000256|ARBA:ARBA00006669}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHO67124.1}.
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DR EMBL; AGWK01000047; EHO67124.1; -; Genomic_DNA.
DR AlphaFoldDB; H1Q4E8; -.
DR STRING; 883158.HMPREF9140_01786; -.
DR PATRIC; fig|883158.3.peg.1783; -.
DR eggNOG; COG1564; Bacteria.
DR eggNOG; COG3201; Bacteria.
DR HOGENOM; CLU_675897_0_0_10; -.
DR Proteomes; UP000016023; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0034257; F:nicotinamide riboside transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0004788; F:thiamine diphosphokinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR CDD; cd07995; TPK; 1.
DR Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic domain; 1.
DR InterPro; IPR006419; NMN_transpt_PnuC.
DR InterPro; IPR006282; Thi_PPkinase.
DR InterPro; IPR049442; Thi_PPkinase-like_C.
DR InterPro; IPR007371; TPK_catalytic.
DR InterPro; IPR036759; TPK_catalytic_sf.
DR NCBIfam; TIGR01528; NMN_trans_PnuC; 1.
DR NCBIfam; TIGR01378; thi_PPkinase; 1.
DR PANTHER; PTHR36122; NICOTINAMIDE RIBOSIDE TRANSPORTER PNUC; 1.
DR PANTHER; PTHR36122:SF2; NICOTINAMIDE RIBOSIDE TRANSPORTER PNUC; 1.
DR Pfam; PF04973; NMN_transporter; 1.
DR Pfam; PF21275; Thi_PPkinase_C; 1.
DR Pfam; PF04263; TPK_catalytic; 1.
DR SUPFAM; SSF63999; Thiamin pyrophosphokinase, catalytic domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016023};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 30..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 222..319
FT /note="Thiamin pyrophosphokinase catalytic"
FT /evidence="ECO:0000259|Pfam:PF04263"
FT DOMAIN 332..400
FT /note="Thiamin pyrophosphokinase-like substrate-binding"
FT /evidence="ECO:0000259|Pfam:PF21275"
SQ SEQUENCE 407 AA; 46883 MW; 4C05CBA3B78BF686 CRC64;
MQEFISTHWL DLLGTLIGLV YIYQEYKASI WLWLTGIVMP VVYMFVYYEA GLYADFGMQI
YYALAAIYGF LFWKLGRHEQ KELPVSHFPR RLVLPATAVF FVLWGALWLV LVKFTNSTVP
VLDSFGNALS FIGLWALARK YIEQWWIWIV VDLELSTLYI YKDIPFTAVL YALYAVIAVA
GYRKWKRDYK ADIRHEGQLP SDGVVILAAG DFPRHEVPLA ILRKAKELYV CDGALAELIE
YGLEPTAVIG DGDSISPSLR ERYKEIYHQF DEQDDNDLTK ATRFALTRTS ERNFIYLGAT
GKRENHTLGN ISLLMRYRRE LGVCPVMITD HGWFCPSSGN TEFCSFAGQQ VSIFNISCRQ
LSSYGLKWPA YPFKEQWQGT LNEALGPRFT VYADGDYLVY RTHEPKL
//
